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Enzymatic glycosylation of small molecules: challenging substrates require tailored catalysts

(2012) CHEMISTRY-A EUROPEAN JOURNAL. 18(35). p.10786-10801
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Biotechnology for a sustainable economy (Bio-Economy)
Abstract
Glycosylation can significantly improve the physicochemical and biological properties of small molecules like vitamins, antibiotics, flavors, and fragrances. The chemical synthesis of glycosides is, however, far from trivial and involves multistep routes that generate lots of waste. In this review, biocatalytic alternatives are presented that offer both stricter specificities and higher yields. The advantages and disadvantages of different enzyme classes are discussed and illustrated with a number of recent examples. Progress in the field of enzyme engineering and screening are expected to result in new applications of biocatalytic glycosylation reactions in various industrial sectors.
Keywords
acceptor specificity, enzyme engineering, glycosylation, glycosyltransferase, high-throughput screening, BETA-N-ACETYLHEXOSAMINIDASE, APPENDED BIPYRIDINIUM SALTS, LACTOBACILLUS-REUTERI 121, KOENIGS-KNORR REACTIONS, LEUCONOSTOC-MESENTEROIDES B-1299CB, RECOMBINANT SUCROSE PHOSPHORYLASE, ANOMER-SELECTIVE-GLUCOSYLATION, INVERTING GLYCOSIDE HYDROLASE, GLYCOSYNTHASE-TYPE REACTION, ACID-SUBSTITUTED VIOLOGENS

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Citation

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MLA
Desmet, Tom, Wim Soetaert, Pavla Bojarová , et al. “Enzymatic Glycosylation of Small Molecules: Challenging Substrates Require Tailored Catalysts.” CHEMISTRY-A EUROPEAN JOURNAL 18.35 (2012): 10786–10801. Print.
APA
Desmet, Tom, Soetaert, W., Bojarová , P., Křen, V., Dijkhuizen, L., Eastwick-Field , V., & Schiller, A. (2012). Enzymatic glycosylation of small molecules: challenging substrates require tailored catalysts. CHEMISTRY-A EUROPEAN JOURNAL, 18(35), 10786–10801.
Chicago author-date
Desmet, Tom, Wim Soetaert, Pavla Bojarová , Vladimir Křen, Lubbert Dijkhuizen, Vanessa Eastwick-Field , and Alexander Schiller. 2012. “Enzymatic Glycosylation of Small Molecules: Challenging Substrates Require Tailored Catalysts.” Chemistry-a European Journal 18 (35): 10786–10801.
Chicago author-date (all authors)
Desmet, Tom, Wim Soetaert, Pavla Bojarová , Vladimir Křen, Lubbert Dijkhuizen, Vanessa Eastwick-Field , and Alexander Schiller. 2012. “Enzymatic Glycosylation of Small Molecules: Challenging Substrates Require Tailored Catalysts.” Chemistry-a European Journal 18 (35): 10786–10801.
Vancouver
1.
Desmet T, Soetaert W, Bojarová P, Křen V, Dijkhuizen L, Eastwick-Field V, et al. Enzymatic glycosylation of small molecules: challenging substrates require tailored catalysts. CHEMISTRY-A EUROPEAN JOURNAL. 2012;18(35):10786–801.
IEEE
[1]
T. Desmet et al., “Enzymatic glycosylation of small molecules: challenging substrates require tailored catalysts,” CHEMISTRY-A EUROPEAN JOURNAL, vol. 18, no. 35, pp. 10786–10801, 2012.
@article{2974634,
  abstract     = {Glycosylation can significantly improve the physicochemical and biological properties of small molecules like vitamins, antibiotics, flavors, and fragrances. The chemical synthesis of glycosides is, however, far from trivial and involves multistep routes that generate lots of waste. In this review, biocatalytic alternatives are presented that offer both stricter specificities and higher yields. The advantages and disadvantages of different enzyme classes are discussed and illustrated with a number of recent examples. Progress in the field of enzyme engineering and screening are expected to result in new applications of biocatalytic glycosylation reactions in various industrial sectors.},
  author       = {Desmet, Tom and Soetaert, Wim and Bojarová , Pavla and Křen, Vladimir and Dijkhuizen, Lubbert and Eastwick-Field , Vanessa and Schiller, Alexander},
  issn         = {0947-6539},
  journal      = {CHEMISTRY-A EUROPEAN JOURNAL},
  keywords     = {acceptor specificity,enzyme engineering,glycosylation,glycosyltransferase,high-throughput screening,BETA-N-ACETYLHEXOSAMINIDASE,APPENDED BIPYRIDINIUM SALTS,LACTOBACILLUS-REUTERI 121,KOENIGS-KNORR REACTIONS,LEUCONOSTOC-MESENTEROIDES B-1299CB,RECOMBINANT SUCROSE PHOSPHORYLASE,ANOMER-SELECTIVE-GLUCOSYLATION,INVERTING GLYCOSIDE HYDROLASE,GLYCOSYNTHASE-TYPE REACTION,ACID-SUBSTITUTED VIOLOGENS},
  language     = {eng},
  number       = {35},
  pages        = {10786--10801},
  title        = {Enzymatic glycosylation of small molecules: challenging substrates require tailored catalysts},
  url          = {http://dx.doi.org/10.1002/chem.201103069},
  volume       = {18},
  year         = {2012},
}

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